9c1b

Crystal structure of GDP-bound human M-RAS protein in crystal form II

spinqualitylabelsall models 9c1b, resolution 2.27Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9c1b is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.27Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Disease RASM_HUMAN Noonan syndrome. The disease is caused by variants affecting the gene represented in this entry. Function RASM_HUMAN Serves as an important signal transducer for a novel upstream stimuli in controlling cell proliferation. Activates the MAP kinase pathway. Publication Abstract from PubMed M-RAS plays a crucial role in the RAF-MEK signaling pathway. When activated by GTP, M-RAS forms a complex with SHOC2 and PP1C, initiating downstream RAF-MEK signal transduction. In this study, the crystal structure of the GDP-bound human M-RAS protein is presented with two forms of crystal packing. Both the full-length and truncated human M-RAS structures aligned well with the high-confidence section of the AlphaFold2-predicted structure with low r.m.s.d., except for the Switch regions. Despite high sequence similarity to the available mouse M-RAS structure, the full-length human M-RAS structure exhibits unique crystal packing. This inactive human M-RAS structure could offer novel insights for the design of selective compounds targeting M-RAS. Crystal structure of the GDP-bound human M-RAS protein in two crystal forms.,Bester SM, Abrahamsen R, Rodrigues Samora L, Wu WI, Mou TC Acta Crystallogr F Struct Biol Commun. 2024 Sep 1;80(Pt 9):220-227. doi: , 10.1107/S2053230X24007969. Epub 2024 Aug 28. PMID:39196705 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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